UniProt Accession

 GRSF1_HUMAN; Q12849; B3KPW0; Q4W5S5; Q6ZST3; Q8IWD6; Q8NBD2 

Genbank Protein ID

 U07231; AK056891; AK090755; AK094806; AK095799; AK097055; AK127161; AC021989; CH471057; CH471057; BC040485 

Genbank Nucleotide ID

 AAC95399.1; BAG51822.1; BAC03513.1; BAG52934.1; BAG53131.1; BAG53414.1; BAC86863.1; AAY40942.1; EAX05631.1; EAX05634.1; AAH40485.1 

Protein Name

 G-rich sequence factor 1 

Protein Synonyms/Alias

 GRSF-1 

Gene Name

 GRSF1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
208	ESEQDVQKALEKHRM	ubiquitination	[1]
242	LMKSLQVKSSPVVND	ubiquitination	[1, 2, 3, 4, 5, 6]
340	VGSYKGKKIASFPTA	ubiquitination	[1]
425	INFFAPLKPVRITME	ubiquitination	[1]
478	LFLNSCPKGK*****	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences. 

Sequence Annotation

 DOMAIN 122 246 RRM 1.
 DOMAIN 250 326 RRM 2.
 DOMAIN 401 480 RRM 3.
 MOD_RES 244 244 Phosphoserine.
 MOD_RES 335 335 Phosphoserine.  

Keyword

 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Mitochondrion; Mitochondrion nucleoid; mRNA processing; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transit peptide; tRNA processing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 480 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0003729; F:mRNA binding; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0009952; P:anterior/posterior pattern specification; IEA:Compara.
 GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Compara.
 GO:0006378; P:mRNA polyadenylation; TAS:ProtInc. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

  

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS